ID D3XAS7_HORVS Unreviewed; 414 AA.
AC D3XAS7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|PIRNR:PIRNR001028};
DE Flags: Fragment;
GN Name=amy2 {ECO:0000313|EMBL:ADC54282.1};
OS Hordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=77009 {ECO:0000313|EMBL:ADC54282.1};
RN [1] {ECO:0000313|EMBL:ADC54282.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mt.Meron-7 {ECO:0000313|EMBL:ADC54282.1};
RA Wang J.R., Wang Y., Chen X., Wei Y.M., Zheng Y.L.;
RT "Diversity of amy2 genes in wild barley populations from Israel.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548,
CC ECO:0000256|PIRNR:PIRNR001028, ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR001028};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028,
CC ECO:0000256|RuleBase:RU003615}.
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DR EMBL; GU269287; ADC54282.1; -; Genomic_DNA.
DR AlphaFoldDB; D3XAS7; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR013775; A-amylase_pln.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF38; ALPHA-AMYLASE ISOZYME 2A; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Germination {ECO:0000256|ARBA:ARBA00022544};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}.
FT DOMAIN 2..343
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 344..404
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADC54282.1"
SQ SEQUENCE 414 AA; 45448 MW; C7698A2AB7F7DA47 CRC64;
HQVLFQGFNW ESWKQSGGWY NMMMGKVDDI AAAGVTHVWL PPPSHSVSNE GYMPGRLYDI
DASKYGNAAE LKSLIGALHG KGVQAIADIV INHRCADYKD NRGIYCIFEG GTSDGRLDWG
PHMICRDDTK YADGTANLDT GADFAAAPDI DHLNDRVQRE LKEWLLWLKS DLGFDAWRLD
FARGYSPEMA KVYIDGTSPS LAVAEVWDNM ATGGDGKPNY DQDAHRQNLV NWVDKVGGAA
SAGMVFDFTT KGILNAAVEG ELWRLIDPQG KAPGVMGWRP AKAVTFVDNH DTGSTQAMWP
FPSDKVMQGY AYILTHPGTP CIFYDHFFNW GFKDEIAALV AIRKRNGITA TSALKILMHE
GDAYVAEIDG KVVVKIGTRY DVGAVIPAGF ATSAHGKDYA VWEKTATAAT LQRS
//
